3cwg: Difference between revisions
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< | ==Unphosphorylated mouse STAT3 core fragment== | ||
<StructureSection load='3cwg' size='340' side='right'caption='[[3cwg]], [[Resolution|resolution]] 3.05Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cwg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CWG FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cwg OCA], [https://pdbe.org/3cwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cwg RCSB], [https://www.ebi.ac.uk/pdbsum/3cwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cwg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/STAT3_MOUSE STAT3_MOUSE] Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. STAT3B interacts with the N-terminal part of JUN to activate such promoters in a cooperative way.<ref>PMID:11294897</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cw/3cwg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cwg ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Signal transducers and activators of transcription (STATs) are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. Here we report a 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment. The overall monomeric structure is very similar to that of the phosphorylated STAT3 core fragment. However, the dimer interface observed in the unphosphorylated STAT1 core fragment structure is absent in the STAT3 structure. Solution studies further demonstrate that the core fragment of STAT3 is primarily monomeric. Mutations corresponding to those in STAT1, which lead to disruption of the core fragment interface and prolonged tyrosine phosphorylation, show little or no effect on the tyrosine phosphorylation kinetics of STAT3. These results highlight the structural and biochemical differences between STAT3 and STAT1, and suggest different regulation mechanisms of these two proteins. | |||
Crystal structure of unphosphorylated STAT3 core fragment.,Ren Z, Mao X, Mertens C, Krishnaraj R, Qin J, Mandal PK, Romanowski MJ, McMurray JS, Chen X Biochem Biophys Res Commun. 2008 Sep 12;374(1):1-5. Epub 2008 Apr 21. PMID:18433722<ref>PMID:18433722</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3cwg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Krishnaraj | [[Category: Krishnaraj R]] | ||
[[Category: Mandal | [[Category: Mandal PK]] | ||
[[Category: Mao | [[Category: Mao X]] | ||
[[Category: McMurray | [[Category: McMurray JS]] | ||
[[Category: Mertens | [[Category: Mertens C]] | ||
[[Category: Qin | [[Category: Qin J]] | ||
[[Category: Ren | [[Category: Ren Z]] | ||
[[Category: Romanowshi | [[Category: Romanowshi MJ]] | ||
Latest revision as of 15:34, 30 August 2023
Unphosphorylated mouse STAT3 core fragmentUnphosphorylated mouse STAT3 core fragment
Structural highlights
FunctionSTAT3_MOUSE Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. STAT3B interacts with the N-terminal part of JUN to activate such promoters in a cooperative way.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSignal transducers and activators of transcription (STATs) are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. Here we report a 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment. The overall monomeric structure is very similar to that of the phosphorylated STAT3 core fragment. However, the dimer interface observed in the unphosphorylated STAT1 core fragment structure is absent in the STAT3 structure. Solution studies further demonstrate that the core fragment of STAT3 is primarily monomeric. Mutations corresponding to those in STAT1, which lead to disruption of the core fragment interface and prolonged tyrosine phosphorylation, show little or no effect on the tyrosine phosphorylation kinetics of STAT3. These results highlight the structural and biochemical differences between STAT3 and STAT1, and suggest different regulation mechanisms of these two proteins. Crystal structure of unphosphorylated STAT3 core fragment.,Ren Z, Mao X, Mertens C, Krishnaraj R, Qin J, Mandal PK, Romanowski MJ, McMurray JS, Chen X Biochem Biophys Res Commun. 2008 Sep 12;374(1):1-5. Epub 2008 Apr 21. PMID:18433722[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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